Other: ADF Domain

Domain Binding and Function

The Actin-Depolymerizing Factor (ADF) homology domain or ADF domain is a 130–170 amino acid domain, first identified in the ADF family of proteins, that is associated with proteins involved in F-actin severing. The domain functions as an actin-binding module present in an extensive family of proteins, including ADF/Cofilin, the Twinfilins and Drebrin/Adp1. This evolutionarily primitive domain pre-dates the divergence of fungi and animals and is found in all eukaryotic organisms. The ADF-containing proteins ADF, Cofilin, Depactin and Actophorin bind to monomeric and filamentous actin and that act to sever Actin filaments. This creates more plus (barbed) and minus (pointed) ends allowing faster Actin turnover and results in the observation that these proteins both rapidly depolymerize filamentous Actin in vitro, as well as increase the rate of F-actin polymerization. Certain ADF-containing proteins appear to have developed more specialized functions as Drebrin/Adp1 class proteins bind only filamentous actin, while Twinfilins bind only monomeric Actin.

Structure Reference

1. Fedorov, A.A. et al. (1997) Nat. Struct. Biol. 4(5), 366–369.

Examples of Domain Proteins

Binding Examples

ADF Domain Protein	Binding Partners
ADF/Cofilin	Filamentous and monomeric actin
Drebrin	Filamentous actin
Twinfilins	Monomeric actin